{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T10:31:36Z","timestamp":1776076296978,"version":"3.50.1"},"reference-count":66,"publisher":"Rockefeller University Press","issue":"4","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,5,18]]},"abstract":"<jats:p>Lateral assemblies of glycolipids and cholesterol, \u201crafts,\u201d have been implicated to play a role in cellular processes like membrane sorting, signal transduction, and cell adhesion. We studied the structure of raft domains in the plasma membrane of non-polarized cells. Overexpressed plasma membrane markers were evenly distributed in the plasma membrane. We compared the patching behavior of pairs of raft markers (defined by insolubility in Triton X-100) with pairs of raft\/non-raft markers. For this purpose we cross-linked glycosyl-phosphatidylinositol (GPI)-anchored proteins placental alkaline phosphatase (PLAP), Thy-1, influenza virus hemagglutinin (HA), and the raft lipid ganglioside GM1 using antibodies and\/or cholera toxin. The patches of these raft markers overlapped extensively in BHK cells as well as in Jurkat T\u2013lymphoma cells. Importantly, patches of GPI-anchored PLAP accumulated src-like protein tyrosine kinase fyn, which is thought to be anchored in the cytoplasmic leaflet of raft domains. In contrast patched raft components and patches of transferrin receptor as a non-raft marker were sharply separated. Taken together, our data strongly suggest that coalescence of cross-linked raft elements is mediated by their common lipid environments, whereas separation of raft and non-raft patches is caused by the immiscibility of different lipid phases. This view is supported by the finding that cholesterol depletion abrogated segregation. Our results are consistent with the view that raft domains in the plasma membrane of non-polarized cells are normally small and highly dispersed but that raft size can be modulated by oligomerization of raft components.<\/jats:p>","DOI":"10.1083\/jcb.141.4.929","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:46:23Z","timestamp":1027701983000},"page":"929-942","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":1004,"title":["Lipid Domain Structure of the Plasma Membrane Revealed by Patching of Membrane Components"],"prefix":"10.1083","volume":"141","author":[{"given":"Thomas","family":"Harder","sequence":"first","affiliation":[{"name":"European Molecular Biology Laboratory, Cell Biology Programme, 69117 Heidelberg, Germany"}]},{"given":"Peter","family":"Scheiffele","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory, Cell Biology Programme, 69117 Heidelberg, Germany"}]},{"given":"Paul","family":"Verkade","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory, Cell Biology Programme, 69117 Heidelberg, Germany"}]},{"given":"Kai","family":"Simons","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory, Cell Biology Programme, 69117 Heidelberg, Germany"}]}],"member":"291","published-online":{"date-parts":[[1998,5,18]]},"reference":[{"key":"2023072207441957400_B1","doi-asserted-by":"crossref","first-page":"10944","DOI":"10.1021\/bi971167g","article-title":"On the origin of sphingolipid\/ cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent insoluble, liquid ordered lipid phase in model membranes","volume":"36","author":"Ahmed","year":"1997","journal-title":"Biochemistry"},{"key":"2023072207441957400_B2","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1084\/jem.176.1.275","article-title":"Major histocompatibility complex restricted recognition of retroviral superantigens by V \u03b2 17+ T cells","volume":"176","author":"Blackman","year":"1992","journal-title":"J Exp Med"},{"key":"2023072207441957400_B3","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1083\/jcb.114.3.413","article-title":"A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin","volume":"114","author":"Brewer","year":"1991","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B4","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/0962-8924(92)90183-N","article-title":"Interactions between GPI-anchored proteins and membrane lipids","volume":"2","author":"Brown","year":"1992","journal-title":"Trends Cell Biol"},{"key":"2023072207441957400_B5","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/0952-7915(93)90052-T","article-title":"The tyrosine kinase connection: how GPI-anchored proteins activate T cells","volume":"5","author":"Brown","year":"1993","journal-title":"Curr Opin Immunol"},{"key":"2023072207441957400_B6","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0092-8674(92)90189-J","article-title":"Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface","volume":"68","author":"Brown","year":"1992","journal-title":"Cell"},{"key":"2023072207441957400_B7","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1126\/science.2571189","article-title":"Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells","volume":"245","author":"Brown","year":"1989","journal-title":"Science"},{"key":"2023072207441957400_B8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1242\/jcs.111.1.1","article-title":"Sphingolipid organisation in biomembranes: what physical studies of model membranes reveal","volume":"111","author":"Brown","year":"1998","journal-title":"J Cell Sci"},{"key":"2023072207441957400_B9","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1099\/0022-1317-64-6-1241","article-title":"Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: presence of Thy-I glycoprotein and absence of H-2, Pgp1 and T-200 glycoproteins on the envelopes of these virus particles","volume":"64","author":"Calafat","year":"1983","journal-title":"J Gen Virol"},{"key":"2023072207441957400_B10","doi-asserted-by":"crossref","first-page":"3150","DOI":"10.1016\/S0021-9258(18)53671-1","article-title":"Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol","volume":"268","author":"Cerneus","year":"1993","journal-title":"J Biol Chem"},{"key":"2023072207441957400_B11","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1083\/jcb.133.4.791","article-title":"Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases","volume":"133","author":"Deckert","year":"1996","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B12","doi-asserted-by":"crossref","first-page":"6838","DOI":"10.1074\/jbc.270.12.6838","article-title":"Caveolin is palmitoylated on multiple cysteine residues: Palmitoylation is not required for localization of caveolin to caveolae","volume":"270","author":"Dietzen","year":"1995","journal-title":"J Biol Chem"},{"key":"2023072207441957400_B13","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1002\/j.1460-2075.1994.tb06437.x","article-title":"VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells","volume":"13","author":"Fiedler","year":"1994","journal-title":"EMBO (Eur Mol Biol Organ) J"},{"key":"2023072207441957400_B14","doi-asserted-by":"crossref","first-page":"4276","DOI":"10.1074\/jbc.272.7.4276","article-title":"Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains","volume":"272","author":"Field","year":"1997","journal-title":"J Biol Chem"},{"key":"2023072207441957400_B15","doi-asserted-by":"crossref","first-page":"8655","DOI":"10.1073\/pnas.92.19.8655","article-title":"De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin","volume":"92","author":"Fra","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"2023072207441957400_B16","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1177\/44.8.8756764","article-title":"GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking","volume":"44","author":"Fujimoto","year":"1996","journal-title":"J Histochem Cytochem"},{"key":"2023072207441957400_B17","doi-asserted-by":"crossref","first-page":"6254","DOI":"10.1074\/jbc.270.11.6254","article-title":"Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes","volume":"270","author":"Hanada","year":"1995","journal-title":"J Biol Chem"},{"key":"2023072207441957400_B18","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1083\/jcb.123.5.1119","article-title":"The subcellular distribution of early endosomes is affected by the annexin II2p112complex","volume":"123","author":"Harder","year":"1993","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B19","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/S0955-0674(97)80030-0","article-title":"Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains","volume":"9","author":"Harder","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"2023072207441957400_B20","doi-asserted-by":"crossref","first-page":"3851","DOI":"10.1021\/bi00011a043","article-title":"Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes","volume":"34","author":"Harris","year":"1995","journal-title":"Biochemistry"},{"key":"2023072207441957400_B21","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1083\/jcb.135.1.37","article-title":"Regulation mechanism of ERM protein\/ plasma membrane association: possible involvement of phosphatidyl inositol turnover and rho-dependent signaling pathway","volume":"135","author":"Hirao","year":"1996","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B22","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1146\/annurev.bb.25.060196.000455","article-title":"Antigen-mediated IgE receptor aggregation and signaling: a window on cell surface structure and dynamics","volume":"25","author":"Holowka","year":"1996","journal-title":"Ann Rev Biophys Biomol Struct"},{"key":"2023072207441957400_B23","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1083\/jcb.97.1.73","article-title":"Role of cholesterol in the capping of surface immunoglobulin receptors on murine lymphocytes","volume":"97","author":"Hoover","year":"1983","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B24","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/0092-8674(95)90078-0","article-title":"Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells","volume":"81","author":"Ikonen","year":"1995","journal-title":"Cell"},{"key":"2023072207441957400_B25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1083\/jcb.94.1.1","article-title":"The concept of lipid domains in membranes","volume":"94","author":"Karnovsky","year":"1982","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B26","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1083\/jcb.140.6.1357","article-title":"Cholesterol is required for surface transport of Influenza virus hemagglutinin","volume":"140","author":"Keller","year":"1998","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B27","doi-asserted-by":"crossref","first-page":"3001","DOI":"10.1242\/jcs.110.24.3001","article-title":"Post-Golgi biosynthetic trafficking","volume":"110","author":"Keller","year":"1998","journal-title":"J Cell Sci"},{"key":"2023072207441957400_B28","doi-asserted-by":"crossref","first-page":"13784","DOI":"10.1021\/bi00042a009","article-title":"Alteration of the myometrial plasma membrane cholesterol content with \u03b2-cyclodextrin modulates the binding affinity of the oxytocin receptor","volume":"34","author":"Klein","year":"1995","journal-title":"Biochemistry"},{"key":"2023072207441957400_B29","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1002\/j.1460-2075.1986.tb04306.x","article-title":"Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface","volume":"5","author":"Kreis","year":"1986","journal-title":"EMBO (Eur Mol Biol Organ) J"},{"key":"2023072207441957400_B30","first-page":"187","article-title":"Guilt by insolubility\u2014does a protein's detergent insolubility reflect caveolar location?","volume":"5","author":"Kurzchalia","year":"1995","journal-title":"Trends Cell Biol"},{"key":"2023072207441957400_B31","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/0092-8674(88)90092-X","article-title":"A single amino acid change in the cytoplasmic domain allows the influenza virus haemagglutinin to be endocytosed through coated pits","volume":"53","author":"Lazarovits","year":"1988","journal-title":"Cell"},{"key":"2023072207441957400_B32","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S1044-5781(06)80084-8","article-title":"Caveolae and human disease: functional roles in transcytosis, potocytosis, signalling, and cell polarity","volume":"6","author":"Lisanti","year":"1995","journal-title":"Semin Dev Biol"},{"key":"2023072207441957400_B33","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/0955-0674(94)90075-2","article-title":"Mechanisms of cell polarity: sorting and transport in epithelial cells","volume":"6","author":"Matter","year":"1994","journal-title":"Curr Opin Cell Biol"},{"key":"2023072207441957400_B34","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/0092-8674(92)90551-M","article-title":"Basolateral sorting of LDL receptor in MDCK cells: the cytoplasmic domain contains two tyrosine-dependent targeting determinants","volume":"71","author":"Matter","year":"1992","journal-title":"Cell"},{"key":"2023072207441957400_B35","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1091\/mbc.6.7.929","article-title":"Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment","volume":"6","author":"Mayor","year":"1995","journal-title":"Mol Biol Cell"},{"key":"2023072207441957400_B36","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1126\/science.7516582","article-title":"Sequestration of GPI- anchored proteins in caveolae triggered by cross-linking","volume":"264","author":"Mayor","year":"1994","journal-title":"Science"},{"key":"2023072207441957400_B37","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1002\/pro.5560030202","article-title":"Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide","volume":"3","author":"Merrit","year":"1994","journal-title":"Protein Science"},{"key":"2023072207441957400_B38","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0014-5793(96)00519-4","article-title":"Oligomerisation of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol","volume":"388","author":"Monier","year":"1996","journal-title":"FEBS (Fed Eur Biochem Soc) Lett"},{"key":"2023072207441957400_B39","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/S0955-0674(97)80056-7","article-title":"Reversible palmitoylation of signaling proteins","volume":"9","author":"Mumby","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"2023072207441957400_B40","doi-asserted-by":"crossref","first-page":"10339","DOI":"10.1073\/pnas.92.22.10339","article-title":"VIP21\/caveolin is a cholesterol-binding protein","volume":"92","author":"Murata","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"2023072207441957400_B41","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1083\/jcb.133.3.543","article-title":"Transport of vesicular stomatitis virus G-protein to the cell surface is signal mediated in polarized and nonpolarized cells","volume":"133","author":"M\u00fcsch","year":"1996","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B42","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1083\/jcb.137.6.1255","article-title":"Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells","volume":"137","author":"Odorizzi","year":"1997","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B43","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0014-4827(88)90257-1","article-title":"The submembraneous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ.","volume":"175","author":"Osborn","year":"1988","journal-title":"Exp Cell Res"},{"key":"2023072207441957400_B44","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1177\/42.2.8288861","article-title":"Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae","volume":"42","author":"Parton","year":"1994","journal-title":"J Histochem Cytochem"},{"key":"2023072207441957400_B45","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/S0955-0674(96)80033-0","article-title":"Caveolae and caveolins","volume":"8","author":"Parton","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"2023072207441957400_B46","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1126\/science.7660120","article-title":"Digging into caveolae","volume":"269","author":"Parton","year":"1995","journal-title":"Science"},{"key":"2023072207441957400_B47","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1083\/jcb.134.6.1427","article-title":"Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling","volume":"134","author":"Pierini","year":"1996","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B48","first-page":"5384","article-title":"Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction","volume":"14","author":"Rodgers","year":"1994","journal-title":"Mol Cell Biol"},{"key":"2023072207441957400_B49","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1126\/science.2672330","article-title":"Morphogenesis of the polarized epithelial cell phenotype","volume":"245","author":"Rodriguez-Boulan","year":"1989","journal-title":"Science"},{"key":"2023072207441957400_B50","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/S0955-0674(97)80028-2","article-title":"The role of lipid signaling in constitutive membrane transport","volume":"9","author":"Roth","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"2023072207441957400_B51","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1242\/jcs.109.2.301","article-title":"Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains","volume":"109","author":"Salo","year":"1996","journal-title":"J Cell Sci"},{"key":"2023072207441957400_B52","doi-asserted-by":"crossref","first-page":"8686","DOI":"10.1073\/pnas.88.19.8686","article-title":"Cholesterol-induced fluid-phase immiscibility in membranes","volume":"88","author":"Sankaram","year":"1991","journal-title":"Proc Natl Acad Sci USA"},{"key":"2023072207441957400_B53","doi-asserted-by":"crossref","first-page":"5501","DOI":"10.1093\/emboj\/16.18.5501","article-title":"Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domains","volume":"16","author":"Scheiffele","year":"1997","journal-title":"EMBO (Eur Mol Biol Organ) J"},{"key":"2023072207441957400_B54","doi-asserted-by":"crossref","first-page":"12130","DOI":"10.1073\/pnas.91.25.12130","article-title":"Interactions between saturated acyl chains confer detergent resistance to lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior","volume":"91","author":"Schroeder","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"2023072207441957400_B55","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1083\/jcb.126.2.353","article-title":"Cysteine(3) of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae","volume":"126","author":"Shenoy-Scaria","year":"1994","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B56","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/42408","article-title":"Sphingolipid-cholesterol rafts in membrane trafficking and signalling","volume":"387","author":"Simons","year":"1997","journal-title":"Nature"},{"key":"2023072207441957400_B57","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1083\/jcb.108.3.821","article-title":"Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts","volume":"108","author":"Skibbens","year":"1989","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B58","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1083\/jcb.99.5.1575","article-title":"Direct visualization of redistribution and capping of fluorescent gangliosides on lymphocytes","volume":"99","author":"Spiegel","year":"1984","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B59","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1083\/jcb.125.4.795","article-title":"Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins","volume":"125","author":"Thomas","year":"1994","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B60","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/0959-440X(93)90071-R","article-title":"Phase topology and percolation in multi-phase bilayers: is the biological membrane a domain mosaic?","volume":"3","author":"Vaz","year":"1993","journal-title":"Curr Opin Struct Biol"},{"key":"2023072207441957400_B61","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1083\/jcb.111.3.987","article-title":"Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells","volume":"111","author":"Wandinger-Ness","year":"1990","journal-title":"J Cell Biol"},{"key":"2023072207441957400_B62","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1074\/jbc.272.4.2116","article-title":"Saturation of the endocytic pathway for the transferrin receptor does not affect the endocytosis of the epidermal growth factor receptor","volume":"272","author":"Warren","year":"1997","journal-title":"J Biol Chem"},{"key":"2023072207441957400_B63","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/S0962-8924(97)01130-6","article-title":"Apical targeting in polarised cells: there's more afloat than rafts","volume":"7","author":"Weimbs","year":"1997","journal-title":"Trends Cell Biol"},{"key":"2023072207441957400_B64","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0009-3084(94)90178-3","article-title":"Lipid domains in model and biological membranes","volume":"73","author":"Welti","year":"1994","journal-title":"Chem Phys Lipids"},{"key":"2023072207441957400_B65","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1091\/mbc.8.6.1159","article-title":"Pamitoylation of p59fyn is reversible and sufficient for plasma membrane association","volume":"8","author":"Wolven","year":"1997","journal-title":"Mol Biol Cell"},{"key":"2023072207441957400_B66","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1083\/jcb.133.2.247","article-title":"Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells","volume":"133","author":"Yoshimori","year":"1996","journal-title":"J Cell Biol"}],"container-title":["The Journal of Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/141\/4\/929\/1491881\/15158.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/141\/4\/929\/1491881\/15158.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T07:45:04Z","timestamp":1690011904000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/141\/4\/929\/15800\/Lipid-Domain-Structure-of-the-Plasma-Membrane"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,5,18]]},"references-count":66,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1998,5,18]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.141.4.929","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,5,18]]}}}